Selection by phage display of a variant mustard trypsin inhibitor toxic against aphids. (Articolo in rivista)

Type
Label
  • Selection by phage display of a variant mustard trypsin inhibitor toxic against aphids. (Articolo in rivista) (literal)
Anno
  • 2003-01-01T00:00:00+01:00 (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#doi
  • 10.1046/j.1365-313X.2003.01645.x (literal)
Alternative label
  • Ceci L.R., Volpicella M., RahbĂ© Y., Gallerani R., Beekwilder J. and Jongsma M.A. (2003)
    Selection by phage display of a variant mustard trypsin inhibitor toxic against aphids.
    in Plant journal (Print)
    (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori
  • Ceci L.R., Volpicella M., RahbĂ© Y., Gallerani R., Beekwilder J. and Jongsma M.A. (literal)
Pagina inizio
  • 557 (literal)
Pagina fine
  • 566 (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroVolume
  • 33 (literal)
Rivista
Note
  • ISI Web of Science (WOS) (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#affiliazioni
  • Institute of Biomembranes and Bioenergetics, CNR, Italy; University pf Bari; Plant Research International, Wageningen (Thje Netherlands). (literal)
Titolo
  • Selection by phage display of a variant mustard trypsin inhibitor toxic against aphids. (literal)
Abstract
  • The mustard trypsin inhibitor, MTI-2, is a potent inhibitor of trypsin with no activity towards chymotrypsin. MTI-2 is toxic for lepidopteran insects, but has low activity against aphids. In an attempt to improve the activity of the inhibitor towards aphids, a library of inhibitor variants was constructed and cloned into the pRlac3 phagemid vector. The library of 9.3 x 107 independent colonies was created by randomisation of a stretch of five consecutive codons in the reactive site. Repeated selection rounds against bovine trypsin and chymotrypsin allowed the identification of novel, MTI-2 derived, antitrypsin and antichymotrypsin inhibitors. Chy8, the selected variant with highest affinity for bovine chymotrypsin (Ki = 32 nm versus >1000 nm for the wild-type) represents the strongest known recombinant chymotrypsin inhibitor of the MTI-2 family. It is highly toxic to nymphs of the aphid Acyrthosiphon pisum, and moderately toxic to nymphs of Aphis gossypii and Myzus persicae. The LC50 of 73 microg ml-1 towards A. pisum is the lowest value known among chymotrypsin inhibitors. The aphicidal activity of Chy8 was improved eightfold compared to the wild-type inhibitor. This demonstrates, for the first time, that bovine chymotrypsin provides a useful template to select engineered proteins highly toxic against these aphids. The selected gene will allow the development of transgenic crops that are protected against sucking insect pests. (literal)
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